SCO2B_MOUSE
ID SCO2B_MOUSE Reviewed; 520 AA.
AC Q9ESL0; Q2HJ06;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase 2B, mitochondrial;
DE EC=2.8.3.5;
DE AltName: Full=3-oxoacid CoA-transferase 2B;
DE AltName: Full=Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 2;
DE Short=SCOT-t2;
DE Flags: Precursor;
GN Name=Oxct2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11090426; DOI=10.1095/biolreprod63.6.1601;
RA Koga M., Tanaka H., Yomogida K., Nozaki M., Tsuchida J., Ohta H.,
RA Nakamura Y., Masai K., Yoshimura Y., Yamanaka M., Iguchi N., Nojima H.,
RA Matsumiya K., Okuyama A., Nihsimune Y.;
RT "Isolation and characterization of a haploid germ cell-specific novel
RT complementary deoxyribonucleic acid; testis-specific homologue of succinyl
RT CoA:3-Oxo acid CoA transferase.";
RL Biol. Reprod. 63:1601-1609(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=15028287; DOI=10.1016/j.ygeno.2003.09.018;
RA Onishi M., Yasunaga T., Tanaka H., Nishimune Y., Nozaki M.;
RT "Gene structure and evolution of testicular haploid germ cell-specific
RT genes, Oxct2a and Oxct2b.";
RL Genomics 83:647-657(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Key enzyme for ketone body catabolism. Transfers the CoA
CC moiety from succinate to acetoacetate. Formation of the enzyme-CoA
CC intermediate proceeds via an unstable anhydride species formed between
CC the carboxylate groups of the enzyme and substrate (By similarity).
CC Probably play and important roles in the energy metabolism of
CC spermatozoa. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate;
CC Xref=Rhea:RHEA:24564, ChEBI:CHEBI:30031, ChEBI:CHEBI:35973,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:90726; EC=2.8.3.5;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10034};
CC -!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA
CC from succinyl-CoA: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis specific. Expressed in late spermatids.
CC Accumulates during spermiogenesis. Also detected in the midpiece of
CC spermatozoa. {ECO:0000269|PubMed:11090426}.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000305}.
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DR EMBL; AB049996; BAB16879.1; -; mRNA.
DR EMBL; AB105455; BAC87739.1; -; Genomic_DNA.
DR EMBL; BC113758; AAI13759.1; -; mRNA.
DR CCDS; CCDS18609.1; -.
DR RefSeq; NP_862907.2; NM_181859.3.
DR AlphaFoldDB; Q9ESL0; -.
DR SMR; Q9ESL0; -.
DR STRING; 10090.ENSMUSP00000099708; -.
DR jPOST; Q9ESL0; -.
DR PaxDb; Q9ESL0; -.
DR PeptideAtlas; Q9ESL0; -.
DR PRIDE; Q9ESL0; -.
DR ProteomicsDB; 256934; -.
DR DNASU; 353371; -.
DR GeneID; 353371; -.
DR KEGG; mmu:353371; -.
DR UCSC; uc008uou.2; mouse.
DR CTD; 353371; -.
DR MGI; MGI:2664115; Oxct2b.
DR eggNOG; KOG3822; Eukaryota.
DR InParanoid; Q9ESL0; -.
DR OrthoDB; 460209at2759; -.
DR PhylomeDB; Q9ESL0; -.
DR TreeFam; TF313991; -.
DR Reactome; R-MMU-77108; Utilization of Ketone Bodies.
DR UniPathway; UPA00929; UER00894.
DR BioGRID-ORCS; 353371; 2 hits in 53 CRISPR screens.
DR PRO; PR:Q9ESL0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9ESL0; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0031514; C:motile cilium; ISA:MGI.
DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0046950; P:cellular ketone body metabolic process; IBA:GO_Central.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:MGI.
DR GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
DR InterPro; IPR012792; 3-oxoacid_CoA-transf_A.
DR InterPro; IPR012791; 3-oxoacid_CoA-transf_B.
DR InterPro; IPR014388; 3-oxoacid_CoA-transferase.
DR InterPro; IPR004165; CoA_trans_fam_I.
DR InterPro; IPR004164; CoA_transf_AS.
DR InterPro; IPR004163; CoA_transf_BS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR13707; PTHR13707; 1.
DR Pfam; PF01144; CoA_trans; 2.
DR PIRSF; PIRSF000858; SCOT-t; 1.
DR SMART; SM00882; CoA_trans; 2.
DR SUPFAM; SSF100950; SSF100950; 2.
DR TIGRFAMs; TIGR02429; pcaI_scoA_fam; 1.
DR TIGRFAMs; TIGR02428; pcaJ_scoB_fam; 1.
DR PROSITE; PS01273; COA_TRANSF_1; 1.
DR PROSITE; PS01274; COA_TRANSF_2; 1.
PE 2: Evidence at transcript level;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 40..520
FT /note="Succinyl-CoA:3-ketoacid coenzyme A transferase 2B,
FT mitochondrial"
FT /id="PRO_0000366211"
FT REGION 280..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 342
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
FT CONFLICT 148
FT /note="C -> G (in Ref. 3; AAI13759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 56592 MW; 487EE325086F28CC CRC64;
MAALRLLAWA LPRGVSALRP RPALPHRLIR RYVSDRSGSV HFYTDPVKAV EGVKDGSTVM
LGGFGLCGIP ENLIGALKTK GVKDLKIVSS NVGVDDFGLG ILLASKQVRR VVCSYLGENA
LCEKLYLAGE LELEMTPQGT LAERIRACGT GVPAFYTPTG YGTLVQEGGS PIRYAPDGHL
ITLSEPREVR EFQGRFYLLE HAIRADFALI KGWKADRSGN VIFRGSARNF NVPMCKAADI
SVVEVEEIVD VGTFAPEDIH IPNIYVDRVI KGPKFEKRIE RLTTRDSKPA PGSKDNDPSR
TRIIKRAALE FQDGMYANLG IGIPVLASNY ISPKMTVYLH SENGILGLGP FPLKNEVDAD
VINAGKQTVT VVPGGCFFAS DDSFAMIRGG HLQLTMLGAM QVSQYGDLAN WMVPGKKVKG
MGGAMDLVSS KKTRVVVTME HCTKTKQPKI LKKCTMPLTG KRCVDLIITE KAVFEVNHSK
GLTLVELWEG SSVDDIKATT ACSFAVSPNL KPMQQIKLDA
